TY  - JOUR
AU  - Mesa-Torres, Noel
AU  - Calvo, Ana C
AU  - Oppici, Elisa
AU  - Titelbaum, Nicholas
AU  - Montioli, Riccardo
AU  - Miranda-Vizuete, Antonio
AU  - Cellini, Barbara
AU  - Salido, Eduardo
AU  - Pey, Angel L
PY  - 2016
DO  - 10.1016/j.bbapap.2016.05.004
SN  - 0006-3002
UR  - http://hdl.handle.net/10668/10080
T2  - Biochimica et biophysica acta
AB  - In humans, glyoxylate is an intermediary product of metabolism, whose concentration is finely balanced. Mutations in peroxisomal alanine:glyoxylate aminotransferase (hAGT1) cause primary hyperoxaluria type 1 (PH1), which results in glyoxylate...
LA  - en
PB  - Elsevier BV
KW  - Conformational disease
KW  - Enzyme kinetics
KW  - Primary hyperoxaluria
KW  - Protein stability
KW  - Substrate specificity
KW  - Adaptation, Biological
KW  - Alanine
KW  - Amino Acid Sequence
KW  - Animals
KW  - Biological Evolution
KW  - Caenorhabditis elegans
KW  - Caenorhabditis elegans Proteins
KW  - Cloning, Molecular
KW  - Dimerization
KW  - Energy Metabolism
KW  - Enzyme Stability
KW  - Escherichia coli
KW  - Gene Expression
KW  - Glyoxylates
KW  - Humans
KW  - Mitochondria
KW  - Mutation
KW  - Peroxisomes
KW  - Protein Structure, Secondary
KW  - Pyridoxal Phosphate
KW  - Recombinant Proteins
KW  - Sequence Alignment
KW  - Species Specificity
KW  - Structural Homology, Protein
KW  - Temperature
KW  - Transaminases
TI  - Caenorhabditis elegans AGXT-1 is a mitochondrial and temperature-adapted ortholog of peroxisomal human AGT1: New insights into between-species divergence in glyoxylate metabolism.
TY  - research article
VL  - 1864
ER  -